| pubmed-article:11567089 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11567089 | lifeskim:mentions | umls-concept:C0040648 | lld:lifeskim |
| pubmed-article:11567089 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:11567089 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:11567089 | lifeskim:mentions | umls-concept:C2263109 | lld:lifeskim |
| pubmed-article:11567089 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:11567089 | pubmed:dateCreated | 2001-9-21 | lld:pubmed |
| pubmed-article:11567089 | pubmed:abstractText | Although it is commonly accepted that binding of mitochondrial transcription factor sc-mtTFB to the mitochondrial RNA polymerase is required for specific transcription initiation in Saccharomyces cerevisiae, its precise role has remained undefined. In the present work, the crystal structure of sc-mtTFB has been determined to 2.6 A resolution. The protein consists of two domains, an N-terminal alpha/beta-domain and a smaller domain made up of four alpha-helices. Contrary to previous predictions, sc-mtTFB does not resemble Escherichia coli sigma-factors but rather is structurally homologous to rRNA methyltransferase ErmC'. This suggests that sc-mtTFB functions as an RNA-binding protein, an observation standing in contradiction to the existing model, which proposed a direct interaction of sc-mtTFB with the mitochondrial DNA promoter. Based on the structure, we propose that the promoter specificity region is located on the mitochondrial RNA polymerase and that binding of sc-mtTFB indirectly mediates interaction of the core enzyme with the promoter site. | lld:pubmed |
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| pubmed-article:11567089 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11567089 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11567089 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11567089 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:11567089 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:11567089 | pubmed:author | pubmed-author:WangB CBC | lld:pubmed |
| pubmed-article:11567089 | pubmed:author | pubmed-author:DaileyH AHA | lld:pubmed |
| pubmed-article:11567089 | pubmed:author | pubmed-author:ChenC JCJ | lld:pubmed |
| pubmed-article:11567089 | pubmed:author | pubmed-author:RosaJ TJT | lld:pubmed |
| pubmed-article:11567089 | pubmed:author | pubmed-author:DaileyT ATA | lld:pubmed |
| pubmed-article:11567089 | pubmed:author | pubmed-author:SchubotF DFD | lld:pubmed |
| pubmed-article:11567089 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11567089 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:11567089 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11567089 | pubmed:authorsComplete | Y | lld:pubmed |
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| pubmed-article:11567089 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:11567089 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11567089 | pubmed:articleTitle | Crystal structure of the transcription factor sc-mtTFB offers insights into mitochondrial transcription. | lld:pubmed |
| pubmed-article:11567089 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602, USA. | lld:pubmed |
| pubmed-article:11567089 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11567089 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:11567089 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:11567089 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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